A modified ACORN to solve protein structures at resolutions of 1.7 A or better.

By Jia-Xing Yao, M. Woolfson, Keith S. Wilson, Eleanor J. Dodson. 2005

26 citations recorded by the source corpus.

ACORN has previously been shown to provide an efficient density-modification procedure for the solution of protein structures using diffraction data to better than 1.3 A. The initial phase set could be obtained from a variety of sources such as the position of a heavy atom, a set of scatterers such as S that had been positioned from anomalous dispersion measurements, a fragment or a very low homology model placed from a molecular-replacement search. Several structures solved using the early version of ACORN have been reported in the literature. Here, the effect of applying the original ACORN procedures at lower resolution is reported and new procedures that yield good-quality maps with data sets of resolution down to 1.7 A are described. These new procedures involve the artificial extension of data to atomic resolution and new density-modification processes that develop density at atomic positions that was previously suppressed. The test calculations were aimed firstly towards a proof of principle using a small fragment of a known structure to demonstrate that the procedure could generate correct density and a derived model in initially empty regions of the cell. Further tests addressed the use of more realistic starting models.

Subfields: Materials Chemistry, Molecular Biology, Radiation

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Overview of the CCP4 suite and current developments (2011, methodology): “ACORN (Jia-xing et al., 2005; Dodson & Woolfson, 2009) uses ab initio methods for the determination of phases starting from a small fragment which could be a single heavy atom.”